期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 19, 期 9, 页码 893-899出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2351
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资金
- US National Science Foundation under NSF [ECS-0335765]
- US National Institutes of Health (NIH) [AI93256, AI67854, AI24755]
- Ragon Institute of MGH, MIT and Harvard
- International AIDS Vaccine Initiative
The trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) spike is a molecular machine that mediates virus entry into host cells and is the sole target for virus-neutralizing antibodies. The mature Env spike results from cleavage of a trimeric glycoprotein precursor, gp160, into three gp120 and three gp41 subunits. Here, we describe an similar to 11-angstrom cryo-EM structure of the trimeric HIV-1 Env precursor in its unliganded state. The three gp120 and three gp41 subunits form a cage-like structure with an interior void surrounding the trimer axis. Interprotomer contacts are limited to the gp41 transmembrane region, the torus-like gp41 ectodomain and a trimer-association domain of gp120 composed of the V1, V2 and V3 variable regions. The cage-like architecture, which is unique among characterized viral envelope proteins, restricts antibody access, reflecting requirements imposed by HIV-1 persistence in the host.
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